Karnitz Larry M, Felts Sara J
Department of Molecular Pharmacology and Experimental Therapeutics, Mayo Clinic College of Medicine, Rochester, MN 55905, USA.
Sci STKE. 2007 May 8;2007(385):pe22. doi: 10.1126/stke.3852007pe22.
Although massive genome sequencing efforts have identified the protein kinases encoded by several eukaryotic genomes and proteomic analyses have begun to determine the kinases expressed in a cell, there is still much to learn about the additional cellular events that shape eukaryotic kinomes. Large-scale analyses in Saccharomyces cerevisiae have indicated that a relatively small subset of kinases requires chaperoning by heat shock protein 90 (Hsp90). However, new evidence suggests that most kinases do require chaperoning and, furthermore, that Cdc37, a chaperone that has Hsp90-dependent and -independent functions, serves as the chaperone for a large portion of the yeast kinome.
尽管大规模的基因组测序工作已经鉴定出了几种真核生物基因组所编码的蛋白激酶，并且蛋白质组学分析也已开始确定细胞中表达的激酶，但对于塑造真核生物激酶组的其他细胞事件，仍有许多有待了解之处。对酿酒酵母的大规模分析表明，相对较小的一部分激酶需要热休克蛋白90（Hsp90）的陪伴。然而，新证据表明，大多数激酶确实需要陪伴，此外，具有Hsp90依赖性和非依赖性功能的伴侣蛋白Cdc37，是酵母激酶组中很大一部分激酶的伴侣蛋白。
